2mbx | pdb_00002mbx

Structure, dynamics and stability of allergen cod parvalbumin Gad m 1 by solution and high-pressure NMR.

spinqualitylabelsall models 2mbx, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mbx is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Gad m 1 is the major allergen from Atlantic cod. It belongs to beta-parvalbumin protein family and is characterized by the presence of two calcium-binding sites so called EF-hand motifs. beta-Parvalbumins such as Gad m 1 are the most important fish allergens and their high cross-reactivity is the cause of the observed polysensitization to various fish species in allergic patients. Despite extensive efforts, the complete elucidation of beta-parvalbumin-IgE complexes has not been achieved yet. Allergen structural studies are essential for the development of novel immunotherapy strategies, including vaccination with hypoallergenic derivatives and chimeric molecules. Here, we report for the first time the NMR study of a beta-parvalbumin: Gad m 1. This report includes: (1)H, (13)C and (15)N resonance assignments of Gad m 1 as well as the second structure information based on the (13)C chemical shifts. (1)H, (1)(3)C and (1)(5)N resonance assignments and second structure information of Gad m 1: a beta-parvalbumin allergen from Atlantic cod (Gadus morhua).,Moraes AH, Ackerbauer D, Kostadinova M, Bublin M, Ferreira F, Almeida FC, Breiteneder H, Valente AP Biomol NMR Assign. 2013 Oct;7(2):133-6. doi: 10.1007/s12104-012-9393-y. Epub 2012, May 15. PMID:22585088 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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